Q9MZT9 · MYC_TUPGL
- ProteinMyc proto-oncogene protein
- GeneMYC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids439 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity).
Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameMyc proto-oncogene protein
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Scandentia > Tupaiidae > Tupaia
Accessions
- Primary accessionQ9MZT9
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Keywords
- Disease
PTM/Processing
Features
Showing features for chain, modified residue, cross-link, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000127304 | 1-439 | Myc proto-oncogene protein | |||
Sequence: MPLNVSFASRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVASFSPRGDDDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPSPARGHSGCSTSSLYLQDLSAAASECIDPSVVFPYPLNDGSSPKPCASPDSTAFSPSSDSLLSSTESSPRASPEPLALHEETPPTTSSDSEEDQEDEEEIDVVSVEKRQPPTKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCASPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEKDLLRKRREQLKHKLEQLRNSCA | ||||||
Modified residue | 6 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 52 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 58 | Phosphothreonine; by GSK3; alternate | ||||
Sequence: T | ||||||
Glycosylation | 58 | O-linked (GlcNAc) threonine; alternate | ||||
Sequence: T | ||||||
Modified residue | 62 | Phosphoserine; by DYRK2, GSK3 and CDK2 | ||||
Sequence: S | ||||||
Modified residue | 71 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 143 | N6-acetyllysine; by PCAF; alternate | ||||
Sequence: K | ||||||
Cross-link | 143 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 148 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 148 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 157 | N6-acetyllysine; by PCAF | ||||
Sequence: K | ||||||
Modified residue | 161 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 275 | N6-acetyllysine; by PCAF | ||||
Sequence: K | ||||||
Modified residue | 293 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 298 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 317 | N6-acetyllysine; by PCAF | ||||
Sequence: K | ||||||
Modified residue | 323 | N6-acetyllysine; by PCAF | ||||
Sequence: K | ||||||
Modified residue | 329 | Phosphoserine; by PIM2; in vitro | ||||
Sequence: S | ||||||
Modified residue | 371 | N6-acetyllysine; by PCAF | ||||
Sequence: K |
Post-translational modification
Phosphorylated by PRKDC (By similarity).
Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity).
Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-62 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity).
Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity).
Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-62 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity).
Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in the nucleolus, both interacting with of FBXW7, leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRPC4AP) complex. Ubiquitinated by UBR5 when not forming a heterodimer with another bHLH protein, leading to its degradation: UBR5 recognizes and binds a degron that is only available upon heterodimer dissociation (By similarity).
Ubiquitinated by TRIM6 in a phosphorylation-independent manner
Ubiquitinated by TRIM6 in a phosphorylation-independent manner
Keywords
- PTM
PTM databases
Interaction
Subunit
Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (By similarity).
Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7. Interacts with PIM2. Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6 (By similarity).
Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (By similarity).
Interacts with CIP2A; leading to the stabilization of MYC (By similarity).
Interacts with NUP205 (By similarity).
Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7. Interacts with PIM2. Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6 (By similarity).
Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (By similarity).
Interacts with CIP2A; leading to the stabilization of MYC (By similarity).
Interacts with NUP205 (By similarity).
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 100-108 | 9aaTAD | ||||
Sequence: EMVTELLGG | ||||||
Region | 203-359 | Disordered | ||||
Sequence: SSPKPCASPDSTAFSPSSDSLLSSTESSPRASPEPLALHEETPPTTSSDSEEDQEDEEEIDVVSVEKRQPPTKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCASPRSSDTEENDKRRTH | ||||||
Compositional bias | 206-233 | Polar residues | ||||
Sequence: KPCASPDSTAFSPSSDSLLSSTESSPRA | ||||||
Compositional bias | 345-359 | Basic and acidic residues | ||||
Sequence: PRSSDTEENDKRRTH | ||||||
Domain | 354-406 | bHLH | ||||
Sequence: DKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSV | ||||||
Motif | 355-364 | UBR5-degron | ||||
Sequence: KRRTHNVLER | ||||||
Region | 413-434 | Leucine-zipper | ||||
Sequence: LISEKDLLRKRREQLKHKLEQL |
Domain
The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Family and domain databases
Sequence
- Sequence statusComplete
- Length439
- Mass (Da)48,543
- Last updated2000-10-01 v1
- ChecksumC98C5AFCD8897E1D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 206-233 | Polar residues | ||||
Sequence: KPCASPDSTAFSPSSDSLLSSTESSPRA | ||||||
Compositional bias | 345-359 | Basic and acidic residues | ||||
Sequence: PRSSDTEENDKRRTH |